Hyperphosphorylation of mutant influenza virus matrix protein, M1, causes its retention in the nucleus
about
Influenza B and C virus NEP (NS2) proteins possess nuclear export activities.Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2)Bioinformatic and comparative localization of Rab proteins reveals functional insights into the uncharacterized GTPases Ypt10p and Ypt11pThe packaging signal of influenza viral RNA molecules.Interactome analysis of the influenza A virus transcription/replication machinery identifies protein phosphatase 6 as a cellular factor required for efficient virus replication.Role of protein kinase C betaII in influenza virus entry via late endosomes.Attenuating mutations of the matrix gene of influenza A/WSN/33 virus.Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins.Influenza virus assembly and lipid raft microdomains: a role for the cytoplasmic tails of the spike glycoproteins.Phosphorylation status of the parvovirus minute virus of mice particle: mapping and biological relevance of the major phosphorylation sites.Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 proteinInfluenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis.A comprehensive map of the influenza A virus replication cycleThe highly conserved arginine residues at positions 76 through 78 of influenza A virus matrix protein M1 play an important role in viral replication by affecting the intracellular localization of M1A Single Amino Acid in the M1 Protein Responsible for the Different Pathogenic Potentials of H5N1 Highly Pathogenic Avian Influenza Virus Strains.Nuclear trafficking of influenza virus ribonuleoproteins in heterokaryonsIntroduction of a temperature-sensitive phenotype into influenza A/WSN/33 virus by altering the basic amino acid domain of influenza virus matrix protein.Association of influenza virus NP and M1 proteins with cellular cytoskeletal elements in influenza virus-infected cells.Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex.Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry.Tyrosine 132 phosphorylation of influenza A virus M1 protein is crucial for virus replication by controlling the nuclear import of M1.Phosphorylation drives an apoptotic protein to activate antiapoptotic genes: paradigm of influenza A matrix 1 protein function.Role for influenza virus envelope cholesterol in virus entry and infection.Influenza virus entry and infection require host cell N-linked glycoprotein.Influenza a viruses with mutations in the m1 helix six domain display a wide variety of morphological phenotypes.Mechanism for inhibition of influenza virus RNA polymerase activity by matrix protein.Modulation of nuclear localization of the influenza virus nucleoprotein through interaction with actin filaments.Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathwayReceptor tyrosine kinase inhibitors block multiple steps of influenza a virus replication.Restriction of viral replication by mutation of the influenza virus matrix protein.Threonine 157 of influenza virus PA polymerase subunit modulates RNA replication in infectious viruses.Basic residues of the helix six domain of influenza virus M1 involved in nuclear translocation of M1 can be replaced by PTAP and YPDL late assembly domain motifs.Serine 3 is critical for phosphorylation at the N-terminal end of the nucleoprotein of influenza virus A/Victoria/3/75.Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions.Matrix protein 1: A comparative in silico study on different strains of influenza A H5N1 Virus.Flu's cues: Exploiting host post-translational modifications to direct the influenza virus replication cycle
P2860
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P2860
Hyperphosphorylation of mutant influenza virus matrix protein, M1, causes its retention in the nucleus
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Hyperphosphorylation of mutant ...... s its retention in the nucleus
@ast
Hyperphosphorylation of mutant ...... s its retention in the nucleus
@en
type
label
Hyperphosphorylation of mutant ...... s its retention in the nucleus
@ast
Hyperphosphorylation of mutant ...... s its retention in the nucleus
@en
prefLabel
Hyperphosphorylation of mutant ...... s its retention in the nucleus
@ast
Hyperphosphorylation of mutant ...... s its retention in the nucleus
@en
P2093
P2860
P1433
P1476
Hyperphosphorylation of mutant ...... s its retention in the nucleus
@en
P2093
P2860
P304
P407
P577
1995-01-01T00:00:00Z